Pregled bibliografske jedinice broj: 757707
Mathematical modeling of (1S, 2S)-1- phenylpropane- 1, 2-diol production process catalyzed by alcohol dehydrogenase from Lactobacillus brevis
Mathematical modeling of (1S, 2S)-1- phenylpropane- 1, 2-diol production process catalyzed by alcohol dehydrogenase from Lactobacillus brevis // Breath Analysis 2014 / Buszewski, B ; Kowalska, J (ur.).
Toruń: Nicolaus Copernicus University, 2014. str. 146-147 (poster, nije recenziran, sažetak, znanstveni)
CROSBI ID: 757707 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Mathematical modeling of (1S, 2S)-1- phenylpropane- 1, 2-diol production process catalyzed by alcohol dehydrogenase from Lactobacillus brevis
Autori
Švarc, Anera ; Valinger, Davor ; Vasić-Rački, Đurđa ; Vrsalović Presečki, Ana
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Breath Analysis 2014
/ Buszewski, B ; Kowalska, J - Toruń : Nicolaus Copernicus University, 2014, 146-147
Skup
Breath Analysis 2014
Mjesto i datum
Toruń, Poljska, 06.07.2014. - 09.07.2014
Vrsta sudjelovanja
Poster
Vrsta recenzije
Nije recenziran
Ključne riječi
chiral diols ; alcoholo dehydrogenase ; coenzyme regeneration
Sažetak
This study describes biocatalytical synthesis of (1S, 2S)-1-phenylpropane-1, 2-diol ((1S, 2S)-1- FPD) from (S)-hidroxypropiophenone ((S)-2- HPP) catalyzed by alcohol dehydrogenase from Lactobacillus brevis (LbADH), that belongs to a group of oxidoreductases whose activity requires the presence of a coenzyme. Because of the high price of the coenzyme, the possibility of coenzyme nicotinamide adenine dinucleotide (NADH) regeneration was examined by using a second enzyme, the formate dehydrogenase from Candida boidinii (CbFDH) which catalyzes the reaction of formate oxidation. The LbADH kinetics of the reduction reaction of (S)-2-HPP was described by the double substrate Michaelis-Menten model with included product-competitive inhibition by the NAD+. The kinetics of the reverse reaction was described by the second-order model. The CbFDH kinetics was described by the double substrate Michaelis-Menten kinetics with NADH and (S)-2-HPP competitive inhibition. The mathematical model was developed based on kinetic results and was validated in a batch reactor in two types of systems: without and with coenzyme regeneration. In the system without coenzyme regeneration the substrate yield was 60%, while in the formate/ CbFDH system the substrate yield was 100%. The deactivation of the main enzyme (LbADH) occurred in the system with coenzyme regeneration and was described by the first-order kinetic.
Izvorni jezik
Engleski
Znanstvena područja
Biotehnologija
POVEZANOST RADA
Ustanove:
Fakultet kemijskog inženjerstva i tehnologije, Zagreb